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Infection and Immunity, July 1999, p. 3376-3382, Vol. 67, No. 7
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Deacylation of Purified Lipopolysaccharides by Cellular and Extracellular Components of a Sterile Rabbit Peritoneal Inflammatory Exudate

Yvette Weinrauch,1 Seth S. Katz,1 Robert S. Munford,2 Peter Elsbach,1,3,* and Jerrold Weiss4

Departments of Microbiology1 and Medicine,3 New York University School of Medicine, New York, New York 10016; Departments of Internal Medicine and Microbiology, University of Texas Southwestern Medical Center, Dallas, Texas2; and Inflammation Program, Departments of Medicine and Microbiology, University of Iowa School of Medicine, Iowa City, Iowa4

Received 22 February 1999/Returned for modification 29 March 1999/Accepted 21 April 1999

The extent to which the mammalian host is capable of enzymatic degradation and detoxification of bacterial lipopolysaccharides (LPS) is still unknown. Partial deacylation of LPS by the enzyme acyloxyacyl hydrolase (AOAH) provides such a mechanism, but its participation in the disposal of LPS under physiological conditions has not been established. In this study, deacylation of isolated radiolabeled LPS by both cellular and extracellular components of a sterile inflammatory peritoneal exudate elicited in rabbits was examined ex vivo. AOAH-like activity, tested under artificial conditions (pH 5.4, 0.1% Triton X-100), was evident in all components of the exudate (mononuclear cells [MNC] > polymorphonuclear leukocytes [PMN] > inflammatory [ascitic] fluid [AF]). Under more physiological conditions, in a defined medium containing purified LPS-binding protein, the LPS-deacylating activity of MNC greatly exceeded that of PMN. In AF, MNC (but not PMN) also produced rapid and extensive CD14-dependent LPS deacylation. Under these conditions, almost all MNC-associated LPS underwent deacylation within 1 h, a rate greatly exceeding that previously found in any cell type. The remaining extracellular LPS was more slowly subject to CD14-independent deacylation in AF. Quantitative analysis showed a comparable release of laurate and myristate but no release of 3-hydroxymyristate, consistent with an AOAH-like activity. These findings suggest a major role for CD14+ MNC and a secondary role for AF in the deacylation of cell-free LPS at extravascular inflammatory sites.

* Corresponding author. Mailing address: Departments of Medicine and Microbiology, New York University School of Medicine, 550 1st Ave., New York, NY 10016. Phone: (212) 263-5633. Fax: (212) 263-8276. E-mail: elsbap01{at}mcrcr.med.nyu.edu.

Infection and Immunity, July 1999, p. 3376-3382, Vol. 67, No. 7
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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